Format

Send to

Choose Destination
Proc Natl Acad Sci U S A. 2010 Jul 13;107(28):12529-34. doi: 10.1073/pnas.1003604107. Epub 2010 Jun 24.

The actin-myosin interface.

Author information

1
Biophysics Group, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. Michael.Lorenz@mpimf-heidelberg.mpg.de

Abstract

In order to understand the mechanism of muscle contraction at the atomic level, it is necessary to understand how myosin binds to actin in a reversible way. We have used a novel molecular dynamics technique constrained by an EM map of the actin-myosin complex at 13-A resolution to obtain an atomic model of the strong-binding (rigor) actin-myosin interface. The constraining force resulting from the EM map during the molecular dynamics simulation was sufficient to convert the myosin head from the initial weak-binding state to the strong-binding (rigor) state. Our actin-myosin model suggests extensive contacts between actin and the myosin head (S1). S1 binds to two actin monomers. The contact surface between actin and S1 has increased dramatically compared with previous models. A number of loops in S1 and actin are involved in establishing the interface. Our model also suggests how the loop carrying the critical Arg 405 Glu mutation in S1 found in a familial cardiomyopathy might be functionally involved.

PMID:
20616041
PMCID:
PMC2906587
DOI:
10.1073/pnas.1003604107
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center